Results 291 to 300 of about 223,254 (334)

Glutathione-S-Transferases

1995
Glutathione S-transferases (GSTs) are a group of phase II detoxification enzymes of wide tissue distribution. They are classified into three groups, alpha, mu, and pi, on the basis of their chromosomal location, isoelectric point, and immunoreactivity.
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Glutathione S-transferases in esophageal cancer

Carcinogenesis, 1993
Glutathione content and glutathione S-transferase enzyme activity as well as isoenzyme composition were studied in normal gastric cardia, normal squamous esophageal epithelium and corresponding malignant tumor of 10 patients with esophageal cancer. Mean values of glutathione (38 +/- 6 versus 36 +/- 12 nmol/mg protein) and glutathione S-transferase ...
W H, Peters, T, Wobbes, H M, Roelofs, J B, Jansen   +3 more
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Human genes for glutathione S-transferases

Human Genetics, 1984
The tissue distribution of different glutathione S-transferases (GST) is analysed by electrophoresis. The existence of GST"e" (erythrocyte), GST3, GST1, and GST2 is confirmed. GST"e" the fastest and most thermolabile of different GST analysed is observed only in erythrocyte cells.
V, Laisney, , Nguyen Van Cong, M S, Gross, J, Frezal   +3 more
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Identity of microsomal glutathione-S-transferases

Molecular and Cellular Biochemistry, 1982
Mouse liver microsomes were prepared by repeated washing, homogenization, and centrifugation until almost no more soluble enzymes were found in the supernatant of the last centrifugation. About 0.09% of the total glutathione S-transferase activity and comparable amount of soluble enzymes were detected in microsomes solubilized with Emulgen 913.
C Y, Lee, J D, McKinney
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Molecular Phylogeny of Glutathione-S-Transferases

DNA and Cell Biology, 1997
The glutathione-S-transferase (GST) protein superfamily is currently composed of nearly 100 sequences. This study documents a greater phylogenetic diversity of GSTs than previously realized. Parsimony and distance phylogenetic methods of GST amino acid sequences yielded virtually the same results. There appear to be at least 25 groups (families) of GST-
M J, Snyder, D R, Maddison
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Glutathione S-transferase in human bile

Clinica Chimica Acta, 1989
Glutathione S-transferase (GST) isoenzymes have been measured by specific radioimmunoassay in human bile samples. GST Mu was found in 50% of samples while GST Pi, GST B1 and GST B2 were present in all samples; GST Pi constituted the major isoenzyme identified.
Howie, A F, Hayes, P C, Bouchier, I A, Hayes, J D, Beckett, G J   +4 more
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Enzymology of Cytosolic Glutathione S- Transferases

1994
Publisher Summary The glutathione S-transferases (GSTs) catalyze a range of reactions of glutathione (GSH) with hydrophobic electrophiles. Their most established role is the glutathione conjugation of electrophiles, which would otherwise cause toxic reactions with macromolecules.
B, Ketterer, L G, Christodoulides
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The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance.

Critical reviews in biochemistry and molecular biology, 1995
J. Hayes, D. Pulford
semanticscholar   +1 more source

The glutathione S-transferases of fish

Fish Physiology and Biochemistry, 1987
Substantial soluble glutathione S-transferase activity and millimolar reduced glutathione (GSH) are present in most tissues of both teleosts and elasmobranchs. The hepatic enzymes of fish conjugate a range of electrophilic substrates with GSH, although their specificities are less broad than those of the transferases in rodent liver.
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Levels of glutathione, glutathione reductase and glutathione S-transferase activities in rat lung and liver.

Biochimica et Biophysica Acta, 1979
M. Moron, J. Depierre, B. Mannervik
semanticscholar   +1 more source